Membrane topology of the di- and tripeptide transport protein of Lactococcus lactis

Biochemistry
A HagtingW N Konings

Abstract

Transport of hydrophilic di- and tripeptides into Lactococcus lactis is mediated by a proton motive force-driven peptide transport protein (DtpT) that shares similarity with eukaryotic peptide transporters, e.g., from kidney and small intestine of rabbit, man, and rat. Hydropathy profiling in combination with the "positive inside rule" predicts for most of the homologous proteins an alpha-helical bundle of 12 transmembrane segments, but the positions of these transmembrane segments and the location of the amino and carboxyl termini are by no means conclusive. The secondary structure of DtpT was investigated by analyzing 42 DtpT-alkaline phosphatase fusion proteins, generated by random or directed fusions of the corresponding genes. These studies confirm the presence of 12 transmembrane segments but refute several other predictions made of the secondary structure. Data obtained from the fusion proteins were substantiated by studying the accessibility of single cysteine mutants in putative cytoplasmic or extracellular loops by membrane (im)permeant sulfhydryl reagents. The deduced topology model of DtpT consists of a bundle of 12 alpha-helixes with a short amino and a large carboxyl terminus, both located at the cytoplasmic site ...Continue Reading

Citations

Apr 5, 2000·Biochimica Et Biophysica Acta·B G Forde
Oct 2, 2013·Proceedings of the National Academy of Sciences of the United States of America·Christian A BippesDaniel J Müller
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